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Protein

Heat shock 70 kDa protein 6

Gene

HSPA6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei73ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 17ATP4
Nucleotide bindingi204 – 206ATP3
Nucleotide bindingi270 – 277ATP8
Nucleotide bindingi341 – 344ATP4

GO - Molecular functioni

  • ATPase activity, coupled Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: BHF-UCL
  • heat shock protein binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • cellular response to heat Source: UniProtKB
  • protein refolding Source: UniProtKB
  • response to unfolded protein Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000173110-MONOMER.
ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 6
Alternative name(s):
Heat shock 70 kDa protein B'
Gene namesi
Name:HSPA6
Synonyms:HSP70B'
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:5239. HSPA6.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • centriole Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi563K → R: Complete loss of in vitro methylation by METTL21A. 1 Publication1

Organism-specific databases

DisGeNETi3310.
OpenTargetsiENSG00000173110.
PharmGKBiPA29505.

Chemistry databases

ChEMBLiCHEMBL3232688.

Polymorphism and mutation databases

BioMutaiHSPA6.
DMDMi34978357.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000782641 – 643Heat shock 70 kDa protein 6Add BLAST643

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei102N6-acetyllysineBy similarity1
Modified residuei136Nitrated tyrosineBy similarity1
Modified residuei330N6-acetyllysine; alternateBy similarity1
Cross-linki330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residuei497PhosphothreonineBy similarity1
Modified residuei563N6,N6,N6-trimethyllysine; by METTL21A; in vitro1 Publication1
Modified residuei563N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei563N6-methyllysine; alternateBy similarity1
Modified residuei626PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP17066.
MaxQBiP17066.
PaxDbiP17066.
PeptideAtlasiP17066.
PRIDEiP17066.

2D gel databases

UCD-2DPAGEP17066.

PTM databases

iPTMnetiP17066.
PhosphoSitePlusiP17066.
SwissPalmiP17066.

Expressioni

Inductioni

Only at higher temperatures, and no basal expression.

Gene expression databases

BgeeiENSG00000173110.
CleanExiHS_HSPA6.
GenevisibleiP17066. HS.

Organism-specific databases

HPAiCAB017452.
HPA028549.
HPA052504.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF1P542742EBI-355106,EBI-710997

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • heat shock protein binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109542. 78 interactors.
IntActiP17066. 40 interactors.
MINTiMINT-1139180.
STRINGi9606.ENSP00000310219.

Structurei

Secondary structure

1643
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 12Combined sources4
Beta strandi15 – 24Combined sources10
Beta strandi27 – 30Combined sources4
Beta strandi38 – 41Combined sources4
Beta strandi44 – 46Combined sources3
Beta strandi51 – 53Combined sources3
Helixi55 – 59Combined sources5
Turni60 – 63Combined sources4
Helixi65 – 67Combined sources3
Helixi72 – 74Combined sources3
Turni75 – 77Combined sources3
Helixi83 – 90Combined sources8
Beta strandi93 – 99Combined sources7
Beta strandi102 – 109Combined sources8
Beta strandi112 – 116Combined sources5
Helixi118 – 137Combined sources20
Beta strandi143 – 148Combined sources6
Helixi154 – 166Combined sources13
Beta strandi170 – 176Combined sources7
Helixi177 – 184Combined sources8
Turni185 – 188Combined sources4
Beta strandi195 – 202Combined sources8
Beta strandi207 – 215Combined sources9
Beta strandi218 – 227Combined sources10
Helixi232 – 251Combined sources20
Helixi259 – 275Combined sources17
Turni276 – 278Combined sources3
Beta strandi280 – 290Combined sources11
Beta strandi293 – 300Combined sources8
Helixi301 – 314Combined sources14
Helixi316 – 326Combined sources11
Helixi330 – 332Combined sources3
Beta strandi334 – 340Combined sources7
Helixi341 – 344Combined sources4
Helixi346 – 355Combined sources10
Turni356 – 358Combined sources3
Turni367 – 369Combined sources3
Helixi370 – 383Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FE1X-ray2.20A/B/C6-385[»]
ProteinModelPortaliP17066.
SMRiP17066.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17066.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP17066.
KOiK03283.
OMAiICRPIFS.
OrthoDBiEOG091G03SF.
PhylomeDBiP17066.
TreeFamiTF105042.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17066-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAPRELAVG IDLGTTYSCV GVFQQGRVEI LANDQGNRTT PSYVAFTDTE
60 70 80 90 100
RLVGDAAKSQ AALNPHNTVF DAKRLIGRKF ADTTVQSDMK HWPFRVVSEG
110 120 130 140 150
GKPKVRVCYR GEDKTFYPEE ISSMVLSKMK ETAEAYLGQP VKHAVITVPA
160 170 180 190 200
YFNDSQRQAT KDAGAIAGLN VLRIINEPTA AAIAYGLDRR GAGERNVLIF
210 220 230 240 250
DLGGGTFDVS VLSIDAGVFE VKATAGDTHL GGEDFDNRLV NHFMEEFRRK
260 270 280 290 300
HGKDLSGNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT
310 320 330 340 350
RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDVVLVG GSTRIPKVQK
360 370 380 390 400
LLQDFFNGKE LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP
410 420 430 440 450
LSLGLETAGG VMTTLIQRNA TIPTKQTQTF TTYSDNQPGV FIQVYEGERA
460 470 480 490 500
MTKDNNLLGR FELSGIPPAP RGVPQIEVTF DIDANGILSV TATDRSTGKA
510 520 530 540 550
NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA KNSLEAHVFH
560 570 580 590 600
VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE
610 620 630 640
LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD
Length:643
Mass (Da):71,028
Last modified:September 19, 2003 - v2
Checksum:iBCE348F0226DB70B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti106 – 108RVC → PVS in CAA36061 (PubMed:2327978).Curated3
Sequence conflicti263R → G in CAA36061 (PubMed:2327978).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06071865P → T.1 PublicationCorresponds to variant rs549201566dbSNPEnsembl.1
Natural variantiVAR_06071995R → Q.1 PublicationCorresponds to variant rs400835dbSNPEnsembl.1
Natural variantiVAR_049605150A → T.1 PublicationCorresponds to variant rs10919224dbSNPEnsembl.1
Natural variantiVAR_049606153N → S.1 PublicationCorresponds to variant rs10919225dbSNPEnsembl.1
Natural variantiVAR_049607154D → N.1 PublicationCorresponds to variant rs10919226dbSNPEnsembl.1
Natural variantiVAR_060720159A → V.1 PublicationCorresponds to variant rs41297702dbSNPEnsembl.1
Natural variantiVAR_049608170N → K.1 PublicationCorresponds to variant rs41297704dbSNPEnsembl.1
Natural variantiVAR_049609173R → P.1 PublicationCorresponds to variant rs41297708dbSNPEnsembl.1
Natural variantiVAR_049610178P → A.1 PublicationCorresponds to variant rs41297710dbSNPEnsembl.1
Natural variantiVAR_049611194E → K.1 PublicationCorresponds to variant rs41297714dbSNPEnsembl.1
Natural variantiVAR_024182198L → F.1 PublicationCorresponds to variant rs63749092dbSNPEnsembl.1
Natural variantiVAR_049612260R → H.Corresponds to variant rs41299256dbSNPEnsembl.1
Natural variantiVAR_060721297T → K.1 PublicationCorresponds to variant rs41297718dbSNPEnsembl.1
Natural variantiVAR_059360336V → F.Corresponds to variant rs417707dbSNPEnsembl.1
Natural variantiVAR_049613464S → I.1 PublicationCorresponds to variant rs388218dbSNPEnsembl.1
Natural variantiVAR_049614471R → H.1 PublicationCorresponds to variant rs41299256dbSNPEnsembl.1
Natural variantiVAR_049615528K → E.1 PublicationCorresponds to variant rs570189dbSNPEnsembl.1
Natural variantiVAR_059361528K → R.Corresponds to variant rs570167dbSNPEnsembl.1
Natural variantiVAR_024183562D → E.1 PublicationCorresponds to variant rs753856dbSNPEnsembl.1
Natural variantiVAR_049616572M → V.Corresponds to variant rs452004dbSNPEnsembl.1
Natural variantiVAR_049617577R → Q.1 PublicationCorresponds to variant rs368844dbSNPEnsembl.1
Natural variantiVAR_049618626T → A.1 PublicationCorresponds to variant rs41299260dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51757 Genomic DNA. Translation: CAA36061.1.
X51758 mRNA. Translation: CAA36062.1.
DQ521571 Genomic DNA. Translation: ABF47108.1.
AL590385 Genomic DNA. Translation: CAI16120.1.
BC004279 mRNA. Translation: AAH04279.1.
BC035665 mRNA. Translation: AAH35665.1.
S78631 Genomic DNA. No translation available.
CCDSiCCDS1231.1.
PIRiS09036.
RefSeqiNP_002146.2. NM_002155.4.
UniGeneiHs.654614.

Genome annotation databases

EnsembliENST00000309758; ENSP00000310219; ENSG00000173110.
GeneIDi3310.
KEGGihsa:3310.
UCSCiuc001gaq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51757 Genomic DNA. Translation: CAA36061.1.
X51758 mRNA. Translation: CAA36062.1.
DQ521571 Genomic DNA. Translation: ABF47108.1.
AL590385 Genomic DNA. Translation: CAI16120.1.
BC004279 mRNA. Translation: AAH04279.1.
BC035665 mRNA. Translation: AAH35665.1.
S78631 Genomic DNA. No translation available.
CCDSiCCDS1231.1.
PIRiS09036.
RefSeqiNP_002146.2. NM_002155.4.
UniGeneiHs.654614.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FE1X-ray2.20A/B/C6-385[»]
ProteinModelPortaliP17066.
SMRiP17066.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109542. 78 interactors.
IntActiP17066. 40 interactors.
MINTiMINT-1139180.
STRINGi9606.ENSP00000310219.

Chemistry databases

ChEMBLiCHEMBL3232688.

PTM databases

iPTMnetiP17066.
PhosphoSitePlusiP17066.
SwissPalmiP17066.

Polymorphism and mutation databases

BioMutaiHSPA6.
DMDMi34978357.

2D gel databases

UCD-2DPAGEP17066.

Proteomic databases

EPDiP17066.
MaxQBiP17066.
PaxDbiP17066.
PeptideAtlasiP17066.
PRIDEiP17066.

Protocols and materials databases

DNASUi3310.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309758; ENSP00000310219; ENSG00000173110.
GeneIDi3310.
KEGGihsa:3310.
UCSCiuc001gaq.4. human.

Organism-specific databases

CTDi3310.
DisGeNETi3310.
GeneCardsiHSPA6.
HGNCiHGNC:5239. HSPA6.
HPAiCAB017452.
HPA028549.
HPA052504.
MIMi140555. gene.
neXtProtiNX_P17066.
OpenTargetsiENSG00000173110.
PharmGKBiPA29505.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP17066.
KOiK03283.
OMAiICRPIFS.
OrthoDBiEOG091G03SF.
PhylomeDBiP17066.
TreeFamiTF105042.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000173110-MONOMER.
ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP17066.
GeneWikiiHSPA6.
GenomeRNAii3310.
PROiP17066.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173110.
CleanExiHS_HSPA6.
GenevisibleiP17066. HS.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHSP76_HUMAN
AccessioniPrimary (citable) accession number: P17066
Secondary accession number(s): Q1HBA8, Q8IYK7, Q9BT95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: September 19, 2003
Last modified: November 30, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.